1SQE

1.5A Crystal Structure Of the protein PG130 from Staphylococcus aureus, Structural genomics

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1sqeb1	Alpha and beta proteins (a+b)	Ferredoxin-like	Dimeric alpha+beta barrel	PG130-like	Hypothetical protein PG130 (SAV0165)	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
B	d1sqeb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
A	d1sqea1	Alpha and beta proteins (a+b)	Ferredoxin-like	Dimeric alpha+beta barrel	PG130-like	Hypothetical protein PG130 (SAV0165)	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)
A	d1sqea2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Staphylococcus aureus ) [TaxId: 1280 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2 Family	PG130-like	8100441	4001439	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Dimeric alpha+beta barrel	8100442	3000089	SCOP2 (2022-06-29)
A	SCOP2B Superfamily	Dimeric alpha+beta barrel	8100442	3000089	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	ABM_1	e1sqeB1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: ABM_1	ECOD (1.6)
A	ABM_1	e1sqeA1	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: ABM_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.70.100	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
A	3.30.70.100	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03992	Antibiotic biosynthesis monooxygenase (ABM)	Antibiotic biosynthesis monooxygenase	This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 (Swiss:Q9X9W3) is suggestive that the other proteins function as mult ...	This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 (Swiss:Q9X9W3) is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	hypothetical protein PG130	oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen heme oxygenase (decyclizing) activity catalytic activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding transition metal ion binding iron ion binding ion binding oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen heme oxygenase (decyclizing) activity catalytic activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding transition metal ion binding iron ion binding ion binding metal ion binding small molecule binding	cellular localization inorganic ion homeostasis iron import into cell homeostatic process transport iron ion transport establishment of localization metal ion transport localization intracellular iron ion homeostasis cellular homeostasis chemical homeostasis intracellular monoatomic cation homeostasis establishment of localization in cell monoatomic ion homeostasis cellular localization inorganic ion homeostasis iron import into cell homeostatic process transport iron ion transport establishment of localization metal ion transport localization intracellular iron ion homeostasis cellular homeostasis chemical homeostasis intracellular monoatomic cation homeostasis establishment of localization in cell monoatomic ion homeostasis intracellular chemical homeostasis transition metal ion transport monoatomic ion transport cellular process monoatomic cation homeostasis monoatomic cation transport intracellular monoatomic ion homeostasis pigment catabolic process pigment metabolic process heme metabolic process catabolic process tetrapyrrole metabolic process heme catabolic process porphyrin-containing compound catabolic process metabolic process porphyrin-containing compound metabolic process tetrapyrrole catabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR007138	Antibiotic biosynthesis monooxygenase domain	Domain
A, B	IPR050404	Heme-degrading monooxygenase	Family
A, B	IPR023953	Heme oxygenase IsdG	Family
A, B	IPR011008	Dimeric alpha-beta barrel	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.